DIK, a novel protein kinase that interacts with protein kinase Cdelta. Cloning, characterization, and gene analysis.

@article{Baehr2000DIKAN,
  title={DIK, a novel protein kinase that interacts with protein kinase Cdelta. Cloning, characterization, and gene analysis.},
  author={Carsten Baehr and Andreas Rohwer and Luise Stempka and Gabriele Rincke and Friedrich Marks and Michael Gschwendt},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 46},
  pages={
          36350-7
        }
}
A novel serine/threonine kinase, termed DIK, was cloned using the yeast two-hybrid system to screen a cDNA library from the human keratinocyte cell line HaCaT with the catalytic domain of rat protein kinase Cdelta (PKCdelta(cat)) cDNA as bait. The predicted 784-amino acid polypeptide with a calculated molecular mass of 86 kDa contains a catalytic kinase domain and a putative regulatory domain with ankyrin-like repeats and a nuclear localization signal. Expression of DIK at the mRNA and protein… CONTINUE READING

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